ID F5YZZ2_MYCSD Unreviewed; 646 AA.
AC F5YZZ2;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Chaperone protein HtpG {ECO:0000256|HAMAP-Rule:MF_00505};
DE AltName: Full=Heat shock protein HtpG {ECO:0000256|HAMAP-Rule:MF_00505};
DE AltName: Full=High temperature protein G {ECO:0000256|HAMAP-Rule:MF_00505};
GN Name=htpG {ECO:0000256|HAMAP-Rule:MF_00505,
GN ECO:0000313|EMBL:AEF35596.1};
GN OrderedLocusNames=JDM601_1596 {ECO:0000313|EMBL:AEF35596.1};
OS Mycolicibacter sinensis (strain JDM601) (Mycobacterium sinense).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacter.
OX NCBI_TaxID=875328 {ECO:0000313|EMBL:AEF35596.1, ECO:0000313|Proteomes:UP000009224};
RN [1] {ECO:0000313|EMBL:AEF35596.1, ECO:0000313|Proteomes:UP000009224}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JDM601 {ECO:0000313|EMBL:AEF35596.1,
RC ECO:0000313|Proteomes:UP000009224};
RX PubMed=21685274; DOI=10.1128/JB.05291-11;
RA Zhang Z.Y., Sun Z.Q., Wang Z.L., Wen Z.L., Sun Q.W., Zhu Z.Q., Song Y.Z.,
RA Zhao J.W., Wang H.H., Zhang S.L., Guo X.K.;
RT "Complete genome sequence of a novel clinical isolate, the nontuberculous
RT Mycobacterium strain JDM601.";
RL J. Bacteriol. 193:4300-4301(2011).
CC -!- FUNCTION: Molecular chaperone. Has ATPase activity. {ECO:0000256|HAMAP-
CC Rule:MF_00505}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00505}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00505}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239, ECO:0000256|HAMAP-Rule:MF_00505}.
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DR EMBL; CP002329; AEF35596.1; -; Genomic_DNA.
DR RefSeq; WP_013828532.1; NC_015576.1.
DR AlphaFoldDB; F5YZZ2; -.
DR STRING; 875328.JDM601_1596; -.
DR KEGG; mjd:JDM601_1596; -.
DR eggNOG; COG0326; Bacteria.
DR HOGENOM; CLU_006684_3_0_11; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000009224; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR CDD; cd16927; HATPase_Hsp90-like; 1.
DR Gene3D; 3.30.230.80; -; 1.
DR Gene3D; 3.40.50.11260; -; 1.
DR Gene3D; 1.20.120.790; Heat shock protein 90, C-terminal domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR HAMAP; MF_00505; HSP90; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR019805; Heat_shock_protein_90_CS.
DR InterPro; IPR037196; HSP90_C.
DR InterPro; IPR001404; Hsp90_fam.
DR InterPro; IPR020575; Hsp90_N.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR PANTHER; PTHR11528:SF97; ENDOPLASMIN; 1.
DR PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR Pfam; PF13589; HATPase_c_3; 1.
DR Pfam; PF00183; HSP90; 1.
DR PIRSF; PIRSF002583; Hsp90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF110942; HSP90 C-terminal domain; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS00298; HSP90; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00505};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00505};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00505};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00505}; Reference proteome {ECO:0000313|Proteomes:UP000009224};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_00505}.
FT DOMAIN 28..188
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 1..352
FT /note="A; substrate-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 353..568
FT /note="B"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 497..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..646
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT COMPBIAS 501..519
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 646 AA; 72760 MW; 000F8D2BD5224ECB CRC64;
MSERVEQLEF QAEARQLLDL MIHSVYSNKD AFLRELISNA SDALDKLRLE AFRNKDLDVD
TSDLHIEIEV DKAARTLTVR DNGVGMSREE VVDLIGTLAR SGTAELRQQL REAQDAKNAA
ASEELIGQFG IGFYSVFMVA DRVEMLTHKA GQSEAIRWES TGDGSYTIES VQDAPQGTSI
TLHLKPEDAE DQLPDYTAEW TIRGLVKKYS DFIAWPIRMQ VERRTPPTEE GGEETVTVET
ETLNSMQALW ARSKDEVAQE EYNEFYKHVA HAWDDPLEVI AMKAEGTFEY QALLFIPSHA
PFDLFNRDAQ VGVQLYVKRV FIMGDCDQLM PEYLRFVKGV VDAADMSLNV SREILQQDRQ
INAIRRRLTK KVLSTIKELQ SQRPEDYRTF WTEFGRVVKE GLLSDFDNQE TLLAISSFAS
THSESEPTTL AEYVGRMKDG QEQIFYATGE SGQQLLKSPH LEAFKAKGYE VLLLTDPVDE
LWVNTVAEFD GKPLQSTAKG EVDLDSEEDK TAHEEQRKEQ EKEFADLIGW LQQTLTEHVK
EVRLSTRLTE SPACLITDTF EMTPALARIY RANGQEVPVG KRILELNPAH PLVTGLRQAH
GERGEDAGLA DTAELLYGTA LLAEGGALED PARFAQLLAQ RLASTI
//
